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Database: UniProt
Entry: A0A2K3UW20_9DEIO
LinkDB: A0A2K3UW20_9DEIO
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ID   A0A2K3UW20_9DEIO        Unreviewed;       958 AA.
AC   A0A2K3UW20;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   Name=sucA {ECO:0000313|EMBL:PNY80716.1};
GN   ORFNames=CVO96_04455 {ECO:0000313|EMBL:PNY80716.1};
OS   Deinococcus koreensis.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=2054903 {ECO:0000313|EMBL:PNY80716.1, ECO:0000313|Proteomes:UP000236379};
RN   [1] {ECO:0000313|EMBL:PNY80716.1, ECO:0000313|Proteomes:UP000236379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SJW1-2 {ECO:0000313|EMBL:PNY80716.1,
RC   ECO:0000313|Proteomes:UP000236379};
RA   Choi A.;
RT   "Deinococcus koreensis sp. nov., a radiation-resistant bacterium isolated
RT   from river water.";
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PNY80716.1}.
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DR   EMBL; PPPD01000001; PNY80716.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K3UW20; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000236379; Unassembled WGS sequence.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   CDD; cd02016; TPP_E1_OGDC_like; 1.
DR   Gene3D; 3.40.50.12470; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR   Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR031717; KGD_C.
DR   InterPro; IPR042179; KGD_C_sf.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR   PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR23152:SF4; 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT DHKTD1, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF16870; OxoGdeHyase_C; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:PNY80716.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236379};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          594..791
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   958 AA;  104775 MW;  F705B04576C17F87 CRC64;
     MLGGVMTVSQ TIMSGANAAF IEGLYEAYLA DPQSVDAGWR AYFDQVRGGA PETAHSPIQR
     AFYDLGQTRR GAAAPAGGAA QGMSGAQQAA GALITSYRVY GHISARSNPL RMRGLPVVPE
     LTPEFYGLTE ADLQEHVRDG PFEGPLREVI AQLQETYCGT IGFEYNYLPA NERQWFQARI
     EQGRGQGRHD LTPGERRRLM QKLTAAEGLE LYLRNKYPGV KRFGLEGGES FIPLVDRIIQ
     QAGRAGVKEV VLGMAHRGRL NTLVNIFGKK PSDLFDEFDG KKKISDDPDV AGDVKYHMGF
     SSDVRTPGGA MHLAMAFNPS HLEIVSPVVH GSVRARQDRR GDTERRTVLP ITVHGDAAVS
     GQGVVMETLN LSRLRGFATG GAVRIVINNQ IGFTISDPRD TRSSRYCTDI AKVANAPVLH
     VNGDDPEAVA FCGDLAVAYR QEFGKDVFID LIGFRRNGHN EGDEPRMTQP IMYREIDQHP
     GARAIYAKAL EESGVLAPGE GDALVAKFRD QLDAGESVVE EMENLAQSAL AVDWKSYTDT
     HWDRDGVSTA VPVEKLTELG LKLAAVPEGF KVHRTIERTV IGPREAMARG EQPLDWGMGE
     MLAYASLLDE GYGVRLVGQD SGRGTFVHRH AVLHDQNAAD PLNEEYMALA HLREGQGRVE
     VVDSTLSEEA VLAFEYGYST SEPKGLVAWE AQFGDFANGA QAVVDQFLSA GESKWQRLSG
     LVMLLPHGYE GAGPEHSSAR LERYLQLCAQ KNMQVVVPSS SAQIFHLLRR QVLRPYRKPL
     IVMTPKSLLR NKQAMSPLNE LSGGRFQEVI GDPEVQKARR VVISSGKLHW ELAEARDADR
     DGYAGTALIR LEQLYPFPAD ALSAELAAHP GAQVVWAQEE PQNQGAWLMI WEDLERVLAP
     GQTLSSATRA RSASTATGYA SVHAREQAAV IATALGEPVQ KEVIQEQKEL AQTAQQDG
//
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